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Function of your protein

is a protein that originates from members of the order Thermoplasmatales, however in this article specifically the Mevalonate 3,5-bisphosphate being studied originated from the species Picrophilus Torridus. The purpose of this protein is to catalyze an elimination reaction in order to remove the 3-phosphate group from mevalonate 3,5-biphosphate and further goes on to decarboxylate the substrate produced thereby removing carboxyl groups from the acidic substrate.

Biological relevance and broader implications

This article’s goal was to test the function and relation of the protein Mevalonate 3,5-bisphosphate and compare it to its homologs. The article seeks to explore the evolutionary changes that the protein has gone through that managed to separate it from its suspected evolutionary predecessors which require ATP to function and allowed it to become ATP-independent. This suspected evolutionary relevance is due to the residual signs of the ATP binding site which are still present in the Mevalonate 3,5-bisphosphate despite the protein being completely ATP-independent.

[Oleic Acid(suspected ligand present)

Important amino acids

The article only really talks about how the ligand, like a fatty acid, lacks an ATP binding site. It also talks about the necessity of the ligand being amphipathic as there are hydrophilic and hydrophobic charges found in the binding site.

Structural highlights

The protein is a dimer that contains per linked molecule. The ARG 148 forms hydrogen bonds that allow it to pair with Oleic Acid, the protein’s ligand. Protein also requires H2O to be present in order to bind its . I found it really interesting that the protein only actually attaches to the ligand via small interaction between ARG 148 and water molecules.